Hoechst 33258, distamycin A,and high mobility group protein I (HMG-I) compete for binding to mouse satellite DNA |
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| Authors: | Marko Z. Radic Michael Saghbini Terry S. Elton Raymond Reeves Barbara A. Hamkalo |
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| Affiliation: | (1) Department of Molecular Biology and Biochemistry, University of California, 92717 Iryine, CA, USA;(2) Department of Biochemistry/Biophysics, Washington State University, 99164 Pullman, WA, USA;(3) Present address: Department of Microbiology and Immunology, Medical College of Pennsylvania, 3300 Henry Avenue, 19129 Philadelphia, PA, USA;(4) Present address: Department of Biology, University of California at San Diego, 92093 La Jolla, CA, USA;(5) Present address: School of Medicine, Hypertension Research Program, University of Alabama at Birmingham, University Station, 35294 Birmingham, AL, USA |
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| Abstract: | The experiments described were designed to test the hypothesis that the (A+T)-specific DNA binding ligands Hoechst 33258 and distamycin A affect the condensation of mouse centromeric heterochromatin by competing for binding to satellite DNA with one or more chromosomal proteins. The studies focused on the nonhistone chromosomal protein HMG-I since its binding properties predict it would be a target for competition. Gel mobility shift assays show that HMG-I forms specific complexes with satellite DNA and that the formation of these complexes is competed for by both Hoechst and distamycin. In addition, methidium propyl EDTA Fe(II) [MPE Fe(II)] footprints of ligand-satellite DNA complexes showed essentially the same protection pattern for both drugs and a similar, but not identical, HMG-I footprint. If these in vitro results reflect the in vivo situation then the incomplete condensation of centromeric heterochromatin observed when mouse cells are grown in the presence of either chemical ligand could be a consequence of competition for binding of HMG-I (and possibly other proteins) to satellite DNA.by E.R. Schmidt |
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